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Q15149

- PLEC_HUMAN

UniProt

Q15149 - PLEC_HUMAN

Protein

Plectin

Gene

PLEC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofibers integrity.2 Publications

    GO - Molecular functioni

    1. ankyrin binding Source: BHF-UCL
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. structural constituent of muscle Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cell junction assembly Source: Reactome
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. hemidesmosome assembly Source: UniProtKB

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_20537. Type I hemidesmosome assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plectin
    Short name:
    PCN
    Short name:
    PLTN
    Alternative name(s):
    Hemidesmosomal protein 1
    Short name:
    HD1
    Plectin-1
    Gene namesi
    Name:PLEC
    Synonyms:PLEC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9069. PLEC.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell junctionhemidesmosome 1 Publication

    GO - Cellular componenti

    1. costamere Source: BHF-UCL
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. focal adhesion Source: HPA
    6. hemidesmosome Source: UniProtKB
    7. intermediate filament cytoskeleton Source: HPA
    8. plasma membrane Source: ProtInc
    9. sarcolemma Source: UniProtKB
    10. sarcoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Epidermolysis bullosa simplex with pyloric atresia (EBS-PA) [MIM:612138]: Autosomal recessive genodermatosis characterized by severe skin blistering at birth and congenital pyloric atresia. Death usually occurs in infancy. This disorder is allelic to MD-EBS.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Epidermolysis bullosa simplex, with muscular dystrophy (MD-EBS) [MIM:226670]: A form of epidermolysis bullosa characterized by the association of blister formation at the level of the hemidesmosome with late-onset muscular dystrophy.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti429 – 4291L → LL in MD-EBS. 1 Publication
    VAR_011336
    Natural varianti1003 – 10053Missing in MD-EBS. 1 Publication
    VAR_011337
    Epidermolysis bullosa simplex, Ogna type (O-EBS) [MIM:131950]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin bruising, skin fragility with non-scarring blistering and small hemorrhagic blisters on hands. At the ultrastructural level, it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS, by the occurrence of blisters originating in basal cells above hemidesmosomes, and abnormal hemidesmosome intracellular attachment plates.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2110 – 21101R → W in O-EBS. 1 Publication
    VAR_015817
    Limb-girdle muscular dystrophy 2Q (LGMD2Q) [MIM:613723]: A form of limb-girdle muscular dystrophy characterized by early childhood onset of proximal muscle weakness. Limb-girdle muscular dystrophies are characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. A 9 bp deletion containing the initiation codon in exon 1f of PLEC have been found in limb-girdle muscular dystrophy patients. The mutation results in deficient expression of isoform 9 and disorganization of the myofibers, without any effect on the skin.

    Keywords - Diseasei

    Disease mutation, Epidermolysis bullosa, Limb-girdle muscular dystrophy

    Organism-specific databases

    MIMi131950. phenotype.
    226670. phenotype.
    612138. phenotype.
    613723. phenotype.
    Orphaneti254361. Autosomal recessive limb-girdle muscular dystrophy type 2Q.
    257. Epidermolysis bullosa simplex with muscular dystrophy.
    158684. Epidermolysis bullosa simplex with pyloric atresia.
    79401. Epidermolysis bullosa simplex, Ogna type.
    PharmGKBiPA33399.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 46844684PlectinPRO_0000078135Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei113 – 1131Phosphothreonine1 Publication
    Modified residuei125 – 1251Phosphoserine3 Publications
    Modified residuei149 – 1491Phosphoserine3 Publications
    Modified residuei720 – 7201Phosphoserine4 Publications
    Modified residuei1435 – 14351Phosphoserine4 Publications
    Modified residuei1721 – 17211Phosphoserine1 Publication
    Modified residuei1725 – 17251N6-acetyllysineBy similarity
    Modified residuei1732 – 17321Phosphoserine1 Publication
    Modified residuei2636 – 26361N6-acetyllysineBy similarity
    Modified residuei3033 – 30331PhosphotyrosineBy similarity
    Modified residuei3053 – 30531N6-acetyllysineBy similarity
    Modified residuei3091 – 30911N6-acetyllysine1 Publication
    Modified residuei3362 – 33621PhosphotyrosineBy similarity
    Modified residuei3420 – 34201N6-acetyllysine1 Publication
    Modified residuei4030 – 40301Phosphothreonine4 Publications
    Modified residuei4382 – 43821Phosphoserine2 Publications
    Modified residuei4384 – 43841PhosphoserineBy similarity
    Modified residuei4385 – 43851Phosphoserine2 Publications
    Modified residuei4386 – 43861Phosphoserine2 Publications
    Modified residuei4389 – 43891Phosphoserine2 Publications
    Modified residuei4390 – 43901Phosphoserine1 Publication
    Modified residuei4391 – 43911Phosphoserine1 Publication
    Modified residuei4392 – 43921Phosphoserine1 Publication
    Modified residuei4396 – 43961Phosphoserine3 Publications
    Modified residuei4400 – 44001Phosphoserine1 Publication
    Modified residuei4411 – 44111Phosphothreonine1 Publication
    Modified residuei4539 – 45391Phosphothreonine; by CDK1By similarity
    Modified residuei4613 – 46131Phosphoserine3 Publications
    Modified residuei4615 – 46151PhosphotyrosineBy similarity
    Modified residuei4618 – 46181Phosphoserine1 Publication
    Modified residuei4622 – 46221Phosphoserine2 Publications
    Modified residuei4626 – 46261Phosphoserine3 Publications
    Modified residuei4642 – 46421Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by CDK1; regulates dissociation from intermediate filaments during mitosis.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15149.
    PaxDbiQ15149.
    PRIDEiQ15149.

    PTM databases

    PhosphoSiteiQ15149.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in muscle, heart, placenta and spinal cord.

    Gene expression databases

    ArrayExpressiQ15149.
    BgeeiQ15149.
    CleanExiHS_PLEC1.
    GenevestigatoriQ15149.

    Organism-specific databases

    HPAiCAB003847.
    HPA025967.
    HPA029906.

    Interactioni

    Subunit structurei

    Homodimer or homotetramer. Interacts (via actin-binding domain) with SYNE3. Interacts (via CH 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A. Interacts with ANK3.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FUSP356374EBI-297903,EBI-400434
    ITGB4P161447EBI-297903,EBI-948678

    Protein-protein interaction databases

    BioGridi111355. 55 interactions.
    IntActiQ15149. 25 interactions.
    MINTiMINT-257064.

    Structurei

    Secondary structure

    1
    4684
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi175 – 19319
    Helixi194 – 1963
    Turni203 – 2097
    Helixi211 – 22111
    Helixi233 – 24917
    Helixi260 – 2634
    Helixi267 – 28216
    Helixi297 – 30812
    Turni309 – 3113
    Helixi322 – 3243
    Helixi328 – 33710
    Helixi339 – 3413
    Helixi344 – 3474
    Helixi352 – 36716
    Helixi375 – 3784
    Beta strandi380 – 3823
    Helixi385 – 39814
    Helixi414 – 44027
    Helixi448 – 46417
    Helixi466 – 48823
    Beta strandi490 – 4923
    Helixi500 – 56263
    Turni563 – 5664
    Helixi572 – 59827
    Helixi604 – 62825
    Helixi656 – 67823
    Helixi685 – 71430
    Helixi715 – 7184
    Helixi721 – 77858
    Helixi788 – 82134
    Helixi827 – 85428
    Helixi893 – 9008
    Helixi904 – 92522
    Helixi932 – 9343
    Beta strandi944 – 9485
    Beta strandi964 – 9707
    Beta strandi975 – 9795
    Beta strandi985 – 9895
    Helixi990 – 9923
    Helixi1000 – 102425
    Helixi1493 – 152735

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MB8X-ray2.15A175-403[»]
    2ODUX-ray2.30A410-640[»]
    2ODVX-ray2.05A410-640[»]
    3F7PX-ray2.75A/B175-403[»]
    3PDYX-ray2.22A/B653-858[»]
    3PE0X-ray2.95A/B750-1028[»]
    4GDOX-ray1.70A/B/C/D/E/F1492-1530[»]
    ProteinModelPortaliQ15149.
    SMRiQ15149. Positions 5-101, 175-400, 413-630, 653-1025, 2782-3023, 3441-3681, 4021-4260, 4412-4605.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15149.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini175 – 400226Actin-bindingAdd
    BLAST
    Domaini179 – 282104CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini295 – 397103CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati645 – 71066Spectrin 1Add
    BLAST
    Repeati740 – 82485Spectrin 2Add
    BLAST
    Repeati837 – 93094Spectrin 3Add
    BLAST
    Repeati1315 – 1415101Spectrin 4Add
    BLAST
    Repeati2826 – 286338Plectin 1Add
    BLAST
    Repeati2864 – 290138Plectin 2Add
    BLAST
    Repeati2902 – 293938Plectin 3Add
    BLAST
    Repeati2940 – 297738Plectin 4Add
    BLAST
    Repeati2981 – 301535Plectin 5Add
    BLAST
    Repeati3116 – 315338Plectin 6Add
    BLAST
    Repeati3154 – 319138Plectin 7Add
    BLAST
    Repeati3192 – 322938Plectin 8Add
    BLAST
    Repeati3230 – 326738Plectin 9Add
    BLAST
    Repeati3268 – 330538Plectin 10Add
    BLAST
    Repeati3306 – 334338Plectin 11Add
    BLAST
    Repeati3485 – 352238Plectin 12Add
    BLAST
    Repeati3523 – 356038Plectin 13Add
    BLAST
    Repeati3561 – 359838Plectin 14Add
    BLAST
    Repeati3599 – 363638Plectin 15Add
    BLAST
    Repeati3640 – 367435Plectin 16Add
    BLAST
    Repeati3820 – 385738Plectin 17Add
    BLAST
    Repeati3858 – 389538Plectin 18Add
    BLAST
    Repeati3896 – 393338Plectin 19Add
    BLAST
    Repeati3934 – 397138Plectin 20Add
    BLAST
    Repeati3975 – 400834Plectin 21Add
    BLAST
    Repeati4063 – 410038Plectin 22Add
    BLAST
    Repeati4101 – 413838Plectin 23Add
    BLAST
    Repeati4139 – 417638Plectin 24Add
    BLAST
    Repeati4177 – 421438Plectin 25Add
    BLAST
    Repeati4218 – 425235Plectin 26Add
    BLAST
    Repeati4265 – 430541Plectin 27Add
    BLAST
    Repeati4319 – 435638Plectin 28Add
    BLAST
    Repeati4408 – 444538Plectin 29Add
    BLAST
    Repeati4446 – 448338Plectin 30Add
    BLAST
    Repeati4484 – 452138Plectin 31Add
    BLAST
    Repeati4522 – 455938Plectin 32Add
    BLAST
    Repeati4560 – 459738Plectin 33Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 14701470Globular 1Add
    BLAST
    Regioni1471 – 27551285Central fibrous rod domainAdd
    BLAST
    Regioni2756 – 46841929Globular 2Add
    BLAST
    Regioni4250 – 430051Binding to intermediate filamentsBy similarityAdd
    BLAST
    Regioni4625 – 4640164 X 4 AA tandem repeats of G-S-R-XAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1469 – 27561288Sequence AnalysisAdd
    BLAST

    Domaini

    The N-terminus interacts with actin, the C-terminus with vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and the C-terminus can bind integrin beta-4.

    Sequence similaritiesi

    Belongs to the plakin or cytolinker family.Curated
    Contains 1 actin-binding domain.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 33 plectin repeats.Curated
    Contains 4 spectrin repeats.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5069.
    HOVERGENiHBG053616.
    InParanoidiQ15149.
    KOiK10388.
    OMAiYLNKDTH.
    PhylomeDBiQ15149.
    TreeFamiTF335163.

    Family and domain databases

    Gene3Di1.10.418.10. 2 hits.
    3.90.1290.10. 7 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR001101. Plectin_repeat.
    IPR005326. S10_plectin_N.
    IPR018159. Spectrin/alpha-actinin.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    PF00681. Plectin. 18 hits.
    PF03501. S10_plectin. 1 hit.
    [Graphical view]
    SMARTiSM00033. CH. 2 hits.
    SM00250. PLEC. 32 hits.
    SM00150. SPEC. 7 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF75399. SSF75399. 8 hits.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    [Graphical view]

    Sequences (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15149-1) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-6

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR     50
    AMASLRARGL VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV 100
    RRPVAMVMPA RRTPHVQAVQ GPLGSPPKRG PLPTEEQRVY RRKELEEVSP 150
    ETPVVPATTQ RTLARPGPEP APATDERDRV QKKTFTKWVN KHLIKAQRHI 200
    SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV QIALDYLRHR 250
    QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK 300
    LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ 350
    TNLENLDQAF SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP 400
    RVPDVQDGVR ANELQLRWQE YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE 450
    IEILWSQFLK FKEMELPAKE ADKNRSKGIY QSLEGAVQAG QLKVPPGYHP 500
    LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM EAGLCEEQLN 550
    QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR 600
    HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR 650
    RPELEDSTLR YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ 700
    SIEEFRAKIE RARSDEGQLS PATRGAYRDC LGRLDLQYAK LLNSSKARLR 750
    SLESLHSFVA AATKELMWLN EKEEEEVGFD WSDRNTNMTA KKESYSALMR 800
    ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ WSWMLQLCCC 850
    IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL 900
    LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC 950
    DYKQVEVTVH KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ 1000
    EAQEAVTRLE AQHQALVTLW HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT 1050
    FRTLKPEEQR QALHSLELHY QAFLRDSQDA GGFGPEDRLM AEREYGSCSH 1100
    HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT VHRLRLPLDK 1150
    EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL 1200
    RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK 1250
    EAQAVPATLP ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL 1300
    QQRHGERDVE VERWRERVAQ LLERWQAVLA QTDVRQRELE QLGRQLRYYR 1350
    ESADPLGAWL QDARRRQEQI QAMPLADSQA VREQLRQEQA LLEEIERHGE 1400
    KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP KVQSGSESVI 1450
    QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA 1500
    EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ 1550
    QKRSIQEELQ QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA 1600
    TERQRGGAEG ELQALRARAE EAEAQKRQAQ EEAERLRRQV QDESQRKRQA 1650
    EVELASRVKA EAEAAREKQR ALQALEELRL QAEEAERRLR QAEVERARQV 1700
    QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV AQLREEAERR 1750
    AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE 1800
    KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ 1850
    ELIRLRAETE QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE 1900
    MEVLLASKAR AEEESRSTSE KSKQRLEAEA GRFRELAEEA ARLRALAEEA 1950
    KRQRQLAEED AARQRAEAER VLAEKLAAIG EATRLKTEAE IALKEKEAEN 2000
    ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD SELERQKGLV 2050
    EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE 2100
    QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER 2150
    LKAKVEEARR LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ 2200
    ELQQTLQQEQ SVLDQLRGEA EAARRAAEEA EEARVQAERE AAQSRRQVEE 2250
    AERLKQSAEE QAQARAQAQA AAEKLRKEAE QEAARRAQAE QAALRQKQAA 2300
    DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN LLDEELQRLK 2350
    AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ 2400
    RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK 2450
    EKMQAVQEAT RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG 2500
    FQRTLEAERQ RQLEMSAEAE RLKLRVAEMS RAQARAEEDA QRFRKQAEEI 2550
    GEKLHRTELA TQEKVTLVQT LEIQRQQSDH DAERLREAIA ELEREKEKLQ 2600
    QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL QRERFIEQEK 2650
    AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE 2700
    EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE 2750
    EVTASQVAAT KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI 2800
    LSAEELQRLA QGHTTVDELA RREDVRHYLQ GRSSIAGLLL KATNEKLSVY 2850
    AALQRQLLSP GTALILLEAQ AASGFLLDPV RNRRLTVNEA VKEGVVGPEL 2900
    HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI RLLEAQIATG 2950
    GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT 3000
    YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP 3050
    FGKFQGKTVT IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV 3100
    EEQEQKGRLC FEGLRSLVPA AELLESRVID RELYQQLQRG ERSVRDVAEV 3150
    DTVRRALRGA NVIAGVWLEE AGQKLSIYNA LKKDLLPSDM AVALLEAQAG 3200
    TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT GYRDPYTGQS 3250
    VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL 3300
    DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS 3350
    EKAARARQEE LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT 3400
    AEQRQELLRQ FRTGKVTVEK VIKILITIVE EVETLRQERL SFSGLRAPVP 3450
    ASELLASGVL SRAQFEQLKD GKTTVKDLSE LGSVRTLLQG SGCLAGIYLE 3500
    DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR NQRLYVHEAV 3550
    KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR 3600
    LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF 3650
    DPNTHENLTY RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET 3700
    RRAFEETQID IPGGGSHGGS TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV 3750
    TKERMIIIII EIIEKTEIIR QQGLASYDYV RRRLTAEDLF EARIISLETY 3800
    NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT LSIYQALKKG 3850
    LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS 3900
    AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR 3950
    LGFHLPLEVA YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR 4000
    CRRDDGTGQL LLPLSDARKL TFRGLRKQIT MEELVRSQVM DEATALQLRE 4050
    GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT KERLSVYQAM KKGIIRPGTA 4100
    FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK LLSAERAVTG 4150
    YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV 4200
    EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ 4250
    TGLCLLPLKE KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI 4300
    DHQTYLELSE QECEWEEITI SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL 4350
    IDRSALDQYR AGTLSITEFA DMLSGNAGGF RSRSSSVGSS SSYPISPAVS 4400
    RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV DNITGQRLLE 4450
    AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR 4500
    TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ 4550
    RGTVDARTAQ KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL 4600
    LEAAAQSTKG YYSPYSVSGS GSTAGSRTGS RTGSRAGSRR GSFDATGSGF 4650
    SMTFSSSSYS SSGYGRRYAS GSSASLGGPE SAVA 4684
    Length:4,684
    Mass (Da):531,791
    Last modified:October 14, 2008 - v3
    Checksum:i04772E4F70A304C8
    GO
    Isoform 2 (identifier: Q15149-2) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-1, 1c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA

    Note: Contains a phosphoserine at position 42.

    Show »
    Length:4,574
    Mass (Da):518,473
    Checksum:i7EAEA5A83DEF52EA
    GO
    Isoform 3 (identifier: Q15149-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA
         409-412: Missing.

    Note: Contains a phosphoserine at position 42.

    Show »
    Length:4,570
    Mass (Da):518,032
    Checksum:iA0AF260B8C095C8D
    GO
    Isoform 4 (identifier: Q15149-4) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-11, 1a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-174: MVAGMLMPRD...RPGPEPAPAT → MSQHQLRVPQ...AVLRASEGKK

    Note: Contains a phosphotyrosine at position 26 (By similarity). Contains a phosphoserine at position 21. Contains a phosphoserine at position 20.By similarity

    Show »
    Length:4,547
    Mass (Da):516,198
    Checksum:i0A1A2AB2E557110A
    GO
    Isoform 5 (identifier: Q15149-5) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-8, 1b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-137: Missing.
         138-174: RVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT → MEPSGSLFPSLVVVGHVVTLAAVWHWRRGRRWAQDEQ

    Show »
    Length:4,547
    Mass (Da):516,276
    Checksum:i0EC98F109B723779
    GO
    Isoform 6 (identifier: Q15149-6) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-10, 1g

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.
         134-174: TEEQRVYRRK...RPGPEPAPAT → MSGAGGAFAS...GYLYQQLCCV

    Show »
    Length:4,551
    Mass (Da):516,479
    Checksum:iC2E0FDA51BC17BF2
    GO
    Isoform 7 (identifier: Q15149-7) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-7, 1d

    The sequence of this isoform differs from the canonical sequence as follows:
         1-169: Missing.
         170-174: PAPAT → MKIVP

    Show »
    Length:4,515
    Mass (Da):512,604
    Checksum:iC8701AD6D1C1B26E
    GO
    Isoform 8 (identifier: Q15149-8) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-3, 1e

    The sequence of this isoform differs from the canonical sequence as follows:
         1-159: Missing.
         160-174: QRTLARPGPEPAPAT → MDPSRAIQNEISSLK

    Show »
    Length:4,525
    Mass (Da):513,706
    Checksum:i37A4DFAB46C3B4DD
    GO
    Isoform 9 (identifier: Q15149-9) [UniParc]FASTAAdd to Basket

    Also known as: Plectin-2, 1f

    The sequence of this isoform differs from the canonical sequence as follows:
         1-151: Missing.
         152-174: TPVVPATTQRTLARPGPEPAPAT → MAGPLPDEQDFIQAYEEVREKYK

    Show »
    Length:4,533
    Mass (Da):514,775
    Checksum:i5D6382389A66B955
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711Y → F in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti94 – 941P → A in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti139 – 1391V → L in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti185 – 1851F → S in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti259 – 2591N → D in AAB05427. (PubMed:8698233)Curated
    Sequence conflicti259 – 2591N → D in AAB05428. (PubMed:8698233)Curated
    Sequence conflicti550 – 5501N → H in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti560 – 5601V → I in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti706 – 7061R → Q in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti886 – 8861Y → N in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti1002 – 10021A → V in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti1309 – 13091V → L in AAB05427. (PubMed:8698233)Curated
    Sequence conflicti1309 – 13091V → L in AAB05428. (PubMed:8698233)Curated
    Sequence conflicti1334 – 13341V → L in AAB05427. (PubMed:8698233)Curated
    Sequence conflicti1334 – 13341V → L in AAB05428. (PubMed:8698233)Curated
    Sequence conflicti1534 – 15341M → I in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti1662 – 16621A → T in AAB05427. (PubMed:8698233)Curated
    Sequence conflicti1662 – 16621A → T in AAB05428. (PubMed:8698233)Curated
    Sequence conflicti1688 – 16903RLR → WLC in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti1767 – 17671E → Q in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti1789 – 17891A → L in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti1910 – 19101R → K in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti2154 – 21541K → N in AAB05427. (PubMed:8698233)Curated
    Sequence conflicti2154 – 21541K → N in AAB05428. (PubMed:8698233)Curated
    Sequence conflicti2154 – 21541K → N in CAA65765. (PubMed:8698233)Curated
    Sequence conflicti2154 – 21541K → N in AAR95680. (PubMed:14672974)Curated
    Sequence conflicti2154 – 21541K → N in AAR95682. (PubMed:14672974)Curated
    Sequence conflicti2154 – 21541K → N in AAR95683. (PubMed:14672974)Curated
    Sequence conflicti2160 – 21601R → S in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti2215 – 22151Q → R in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti2244 – 22441S → A in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti2244 – 22441S → A in AAB05427. (PubMed:8698233)Curated
    Sequence conflicti2244 – 22441S → A in AAB05428. (PubMed:8698233)Curated
    Sequence conflicti2244 – 22441S → A in CAA65765. (PubMed:8698233)Curated
    Sequence conflicti3027 – 30271K → E in AAB05427. (PubMed:8698233)Curated
    Sequence conflicti3027 – 30271K → E in AAB05428. (PubMed:8698233)Curated
    Sequence conflicti3310 – 33101A → E in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3361 – 33611L → F in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3408 – 34081L → F in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3447 – 34471A → S in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3531 – 35311A → G in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3580 – 35801S → R in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3589 – 35891Q → K in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3596 – 35961Q → E in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3616 – 36161H → N in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3686 – 36861A → V in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3786 – 37861A → G in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3808 – 38081R → K in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3816 – 38161A → G in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3821 – 38211C → F in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3915 – 39151Q → K in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti3999 – 39991R → K in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti4007 – 40071T → S in CAA91196. (PubMed:8633055)Curated
    Sequence conflicti4467 – 44671F → L in CAA91196. (PubMed:8633055)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti429 – 4291L → LL in MD-EBS. 1 Publication
    VAR_011336
    Natural varianti641 – 6411A → V.
    Corresponds to variant rs11136336 [ dbSNP | Ensembl ].
    VAR_053585
    Natural varianti1003 – 10053Missing in MD-EBS. 1 Publication
    VAR_011337
    Natural varianti1321 – 13211L → V.1 Publication
    Corresponds to variant rs3135109 [ dbSNP | Ensembl ].
    VAR_060088
    Natural varianti1386 – 13861R → Q.
    Corresponds to variant rs11136334 [ dbSNP | Ensembl ].
    VAR_060089
    Natural varianti1459 – 14591H → R.
    Corresponds to variant rs55895668 [ dbSNP | Ensembl ].
    VAR_062133
    Natural varianti2110 – 21101R → W in O-EBS. 1 Publication
    VAR_015817
    Natural varianti2150 – 21501R → W.
    Corresponds to variant rs34893635 [ dbSNP | Ensembl ].
    VAR_053586
    Natural varianti2194 – 21941A → V.
    Corresponds to variant rs7002002 [ dbSNP | Ensembl ].
    VAR_053587
    Natural varianti2791 – 27911S → P.
    Corresponds to variant rs7833924 [ dbSNP | Ensembl ].
    VAR_053588
    Natural varianti2821 – 28211R → W.
    Corresponds to variant rs35723243 [ dbSNP | Ensembl ].
    VAR_053589
    Natural varianti2969 – 29691R → H.
    Corresponds to variant rs6558407 [ dbSNP | Ensembl ].
    VAR_053590
    Natural varianti3162 – 31621V → I.
    Corresponds to variant rs35027700 [ dbSNP | Ensembl ].
    VAR_053591
    Natural varianti3171 – 31711A → V.
    Corresponds to variant rs35858667 [ dbSNP | Ensembl ].
    VAR_053592
    Natural varianti3486 – 34861T → M.
    Corresponds to variant rs34725742 [ dbSNP | Ensembl ].
    VAR_053593
    Natural varianti3490 – 34901G → A.
    Corresponds to variant rs35261863 [ dbSNP | Ensembl ].
    VAR_053594

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 174174MVAGM…PAPAT → MSGEDAEVRAVSEDVSNGSS GSPSPGDTLPWNLGKTQRSR RSGGGAGSNGSVLDPAERAV IRIA in isoform 2 and isoform 3. 2 PublicationsVSP_005030Add
    BLAST
    Alternative sequencei1 – 174174MVAGM…PAPAT → MSQHQLRVPQPEGLGRKRTS SEDNLYLAVLRASEGKK in isoform 4. 1 PublicationVSP_023510Add
    BLAST
    Alternative sequencei1 – 169169Missing in isoform 7. 1 PublicationVSP_037100Add
    BLAST
    Alternative sequencei1 – 159159Missing in isoform 8. 1 PublicationVSP_037101Add
    BLAST
    Alternative sequencei1 – 151151Missing in isoform 9. 1 PublicationVSP_037102Add
    BLAST
    Alternative sequencei1 – 137137Missing in isoform 5. 1 PublicationVSP_037103Add
    BLAST
    Alternative sequencei1 – 133133Missing in isoform 6. 1 PublicationVSP_037104Add
    BLAST
    Alternative sequencei134 – 17441TEEQR…PAPAT → MSGAGGAFASPREVLLERPC WLDGGCEPARRGYLYQQLCC V in isoform 6. 1 PublicationVSP_037105Add
    BLAST
    Alternative sequencei138 – 17437RVYRR…PAPAT → MEPSGSLFPSLVVVGHVVTL AAVWHWRRGRRWAQDEQ in isoform 5. 1 PublicationVSP_037106Add
    BLAST
    Alternative sequencei152 – 17423TPVVP…PAPAT → MAGPLPDEQDFIQAYEEVRE KYK in isoform 9. 1 PublicationVSP_037107Add
    BLAST
    Alternative sequencei160 – 17415QRTLA…PAPAT → MDPSRAIQNEISSLK in isoform 8. 1 PublicationVSP_037108Add
    BLAST
    Alternative sequencei170 – 1745PAPAT → MKIVP in isoform 7. 1 PublicationVSP_037109
    Alternative sequencei409 – 4124Missing in isoform 3. 1 PublicationVSP_005031

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z54367 Genomic DNA. Translation: CAA91196.1.
    U53204 mRNA. Translation: AAB05427.1.
    U63610, U63609 Genomic DNA. Translation: AAB05428.1.
    X97053 mRNA. Translation: CAA65765.1.
    AY480044 mRNA. Translation: AAR95677.1.
    AY480045 mRNA. Translation: AAR95678.1.
    AY480046 mRNA. Translation: AAR95679.1.
    AY480047 mRNA. Translation: AAR95680.1.
    AY480048 mRNA. Translation: AAR95681.1.
    AY480049 mRNA. Translation: AAR95682.1.
    AY480050 mRNA. Translation: AAR95683.1.
    AY480051 mRNA. Translation: AAR95684.1.
    AC109322 Genomic DNA. No translation available.
    CCDSiCCDS43769.1. [Q15149-2]
    CCDS43770.1. [Q15149-9]
    CCDS43771.1. [Q15149-8]
    CCDS43772.1. [Q15149-1]
    CCDS43773.1. [Q15149-5]
    CCDS43774.1. [Q15149-6]
    CCDS43775.1. [Q15149-4]
    CCDS47936.1. [Q15149-7]
    PIRiC59404. A59404.
    G02520.
    RefSeqiNP_000436.2. NM_000445.4. [Q15149-2]
    NP_958780.1. NM_201378.3. [Q15149-9]
    NP_958781.1. NM_201379.2. [Q15149-8]
    NP_958782.1. NM_201380.3. [Q15149-1]
    NP_958783.1. NM_201381.2. [Q15149-7]
    NP_958784.1. NM_201382.3. [Q15149-5]
    NP_958785.1. NM_201383.2. [Q15149-6]
    NP_958786.1. NM_201384.2. [Q15149-4]
    UniGeneiHs.434248.

    Genome annotation databases

    EnsembliENST00000322810; ENSP00000323856; ENSG00000178209. [Q15149-1]
    ENST00000345136; ENSP00000344848; ENSG00000178209. [Q15149-4]
    ENST00000354589; ENSP00000346602; ENSG00000178209. [Q15149-5]
    ENST00000354958; ENSP00000347044; ENSG00000178209. [Q15149-8]
    ENST00000356346; ENSP00000348702; ENSG00000178209. [Q15149-9]
    ENST00000357649; ENSP00000350277; ENSG00000178209. [Q15149-6]
    ENST00000398774; ENSP00000381756; ENSG00000178209. [Q15149-7]
    ENST00000436759; ENSP00000388180; ENSG00000178209. [Q15149-2]
    ENST00000527096; ENSP00000434583; ENSG00000178209. [Q15149-3]
    GeneIDi5339.
    KEGGihsa:5339.
    UCSCiuc003zab.1. human. [Q15149-4]
    uc003zac.1. human. [Q15149-6]
    uc003zad.2. human. [Q15149-5]
    uc003zae.1. human. [Q15149-7]
    uc003zaf.1. human. [Q15149-1]
    uc003zag.1. human. [Q15149-8]
    uc003zah.2. human. [Q15149-9]
    uc003zaj.2. human. [Q15149-2]

    Polymorphism databases

    DMDMi209572726.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Plectin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z54367 Genomic DNA. Translation: CAA91196.1 .
    U53204 mRNA. Translation: AAB05427.1 .
    U63610 , U63609 Genomic DNA. Translation: AAB05428.1 .
    X97053 mRNA. Translation: CAA65765.1 .
    AY480044 mRNA. Translation: AAR95677.1 .
    AY480045 mRNA. Translation: AAR95678.1 .
    AY480046 mRNA. Translation: AAR95679.1 .
    AY480047 mRNA. Translation: AAR95680.1 .
    AY480048 mRNA. Translation: AAR95681.1 .
    AY480049 mRNA. Translation: AAR95682.1 .
    AY480050 mRNA. Translation: AAR95683.1 .
    AY480051 mRNA. Translation: AAR95684.1 .
    AC109322 Genomic DNA. No translation available.
    CCDSi CCDS43769.1. [Q15149-2 ]
    CCDS43770.1. [Q15149-9 ]
    CCDS43771.1. [Q15149-8 ]
    CCDS43772.1. [Q15149-1 ]
    CCDS43773.1. [Q15149-5 ]
    CCDS43774.1. [Q15149-6 ]
    CCDS43775.1. [Q15149-4 ]
    CCDS47936.1. [Q15149-7 ]
    PIRi C59404. A59404.
    G02520.
    RefSeqi NP_000436.2. NM_000445.4. [Q15149-2 ]
    NP_958780.1. NM_201378.3. [Q15149-9 ]
    NP_958781.1. NM_201379.2. [Q15149-8 ]
    NP_958782.1. NM_201380.3. [Q15149-1 ]
    NP_958783.1. NM_201381.2. [Q15149-7 ]
    NP_958784.1. NM_201382.3. [Q15149-5 ]
    NP_958785.1. NM_201383.2. [Q15149-6 ]
    NP_958786.1. NM_201384.2. [Q15149-4 ]
    UniGenei Hs.434248.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MB8 X-ray 2.15 A 175-403 [» ]
    2ODU X-ray 2.30 A 410-640 [» ]
    2ODV X-ray 2.05 A 410-640 [» ]
    3F7P X-ray 2.75 A/B 175-403 [» ]
    3PDY X-ray 2.22 A/B 653-858 [» ]
    3PE0 X-ray 2.95 A/B 750-1028 [» ]
    4GDO X-ray 1.70 A/B/C/D/E/F 1492-1530 [» ]
    ProteinModelPortali Q15149.
    SMRi Q15149. Positions 5-101, 175-400, 413-630, 653-1025, 2782-3023, 3441-3681, 4021-4260, 4412-4605.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111355. 55 interactions.
    IntActi Q15149. 25 interactions.
    MINTi MINT-257064.

    Chemistry

    BindingDBi Q15149.
    ChEMBLi CHEMBL1293240.

    PTM databases

    PhosphoSitei Q15149.

    Polymorphism databases

    DMDMi 209572726.

    Proteomic databases

    MaxQBi Q15149.
    PaxDbi Q15149.
    PRIDEi Q15149.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322810 ; ENSP00000323856 ; ENSG00000178209 . [Q15149-1 ]
    ENST00000345136 ; ENSP00000344848 ; ENSG00000178209 . [Q15149-4 ]
    ENST00000354589 ; ENSP00000346602 ; ENSG00000178209 . [Q15149-5 ]
    ENST00000354958 ; ENSP00000347044 ; ENSG00000178209 . [Q15149-8 ]
    ENST00000356346 ; ENSP00000348702 ; ENSG00000178209 . [Q15149-9 ]
    ENST00000357649 ; ENSP00000350277 ; ENSG00000178209 . [Q15149-6 ]
    ENST00000398774 ; ENSP00000381756 ; ENSG00000178209 . [Q15149-7 ]
    ENST00000436759 ; ENSP00000388180 ; ENSG00000178209 . [Q15149-2 ]
    ENST00000527096 ; ENSP00000434583 ; ENSG00000178209 . [Q15149-3 ]
    GeneIDi 5339.
    KEGGi hsa:5339.
    UCSCi uc003zab.1. human. [Q15149-4 ]
    uc003zac.1. human. [Q15149-6 ]
    uc003zad.2. human. [Q15149-5 ]
    uc003zae.1. human. [Q15149-7 ]
    uc003zaf.1. human. [Q15149-1 ]
    uc003zag.1. human. [Q15149-8 ]
    uc003zah.2. human. [Q15149-9 ]
    uc003zaj.2. human. [Q15149-2 ]

    Organism-specific databases

    CTDi 5339.
    GeneCardsi GC08M144989.
    GeneReviewsi PLEC.
    H-InvDB HIX0168901.
    HGNCi HGNC:9069. PLEC.
    HPAi CAB003847.
    HPA025967.
    HPA029906.
    MIMi 131950. phenotype.
    226670. phenotype.
    601282. gene.
    612138. phenotype.
    613723. phenotype.
    neXtProti NX_Q15149.
    Orphaneti 254361. Autosomal recessive limb-girdle muscular dystrophy type 2Q.
    257. Epidermolysis bullosa simplex with muscular dystrophy.
    158684. Epidermolysis bullosa simplex with pyloric atresia.
    79401. Epidermolysis bullosa simplex, Ogna type.
    PharmGKBi PA33399.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOVERGENi HBG053616.
    InParanoidi Q15149.
    KOi K10388.
    OMAi YLNKDTH.
    PhylomeDBi Q15149.
    TreeFami TF335163.

    Enzyme and pathway databases

    Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_20537. Type I hemidesmosome assembly.

    Miscellaneous databases

    ChiTaRSi PLEC. human.
    EvolutionaryTracei Q15149.
    GeneWikii Plectin.
    GenomeRNAii 5339.
    NextBioi 20680.
    PROi Q15149.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15149.
    Bgeei Q15149.
    CleanExi HS_PLEC1.
    Genevestigatori Q15149.

    Family and domain databases

    Gene3Di 1.10.418.10. 2 hits.
    3.90.1290.10. 7 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR001101. Plectin_repeat.
    IPR005326. S10_plectin_N.
    IPR018159. Spectrin/alpha-actinin.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF00681. Plectin. 18 hits.
    PF03501. S10_plectin. 1 hit.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    SM00250. PLEC. 32 hits.
    SM00150. SPEC. 7 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF75399. SSF75399. 8 hits.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)."
      Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.
      Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), DISEASE, VARIANT VAL-1321.
    3. "Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation."
      Zhang T., Haws P., Wu Q.
      Genome Res. 14:79-89(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7; 8 AND 9).
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Tissue: Ovarian carcinoma.
    6. "Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
      Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
      J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH COL17A1, SUBCELLULAR LOCATION.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1721; THR-4030 AND THR-4411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-4382; SER-4385; SER-4386; SER-4389; SER-4390; SER-4391; SER-4392; SER-4396; SER-4613; SER-4622; SER-4626 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
      Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
      J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOR1A.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; THR-4030 AND SER-4626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386; SER-4389; SER-4396; SER-4613; SER-4618 AND SER-4626, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3091 AND LYS-3420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limb-girdle muscular dystrophy."
      Gundesli H., Talim B., Korkusuz P., Balci-Hayta B., Cirak S., Akarsu N.A., Topaloglu H., Dincer P.
      Am. J. Hum. Genet. 87:834-841(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ISOFORM 9, INVOLVEMENT IN LGMD2Q.
    19. "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
      Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
      Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DST.
    20. "Plectin deficiency leads to both muscular dystrophy and pyloric atresia in epidermolysis bullosa simplex."
      Natsuga K., Nishie W., Shinkuma S., Arita K., Nakamura H., Ohyama M., Osaka H., Kambara T., Hirako Y., Shimizu H.
      Hum. Mutat. 31:E1687-E1698(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MD-EBS AND EBS-PA.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-125; SER-149; SER-720; SER-1435; SER-1732; THR-4030; SER-4382; SER-4396; SER-4400; SER-4613; SER-4622 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C."
      Maiweilidan Y., Klauza I., Kordeli E.
      Exp. Cell Res. 317:724-736(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANK3.
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435 AND THR-4030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain."
      Sonnenberg A., Rojas A.M., de Pereda J.M.
      J. Mol. Biol. 368:1379-1391(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 409-640.
    26. "Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4."
      Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M.
      Structure 11:615-625(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-403.
    27. "Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy."
      Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H., Nishikawa T., McLean W.H.I., Uitto J.
      Hum. Mol. Genet. 5:1539-1546(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MD-EBS 1003-GLN--ALA-1005 DEL.
    28. "A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency."
      Bauer J.W., Rouan F., Kofler B., Rezniczek G.A., Kornacker I., Muss W., Hametner R., Klausegger A., Huber A., Pohla-Gubo G., Wiche G., Uitto J., Hintner H.
      Am. J. Pathol. 158:617-625(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MD-EBS LEU-429 INS.
    29. "A site-specific plectin mutation causes dominant epidermolysis bullosa simplex Ogna: two identical de novo mutations."
      Koss-Harnes D., Hoeyheim B., Anton-Lamprecht I., Gjesti A., Joergensen R.S., Jahnsen F.L., Olaisen B., Wiche G., Gedde-Dahl T. Jr.
      J. Invest. Dermatol. 118:87-93(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT O-EBS TRP-2110.
    30. "Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin."
      Charlesworth A., Gagnoux-Palacios L., Bonduelle M., Ortonne J.-P., De Raeve L., Meneguzzi G.
      J. Invest. Dermatol. 121:1344-1348(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN EBS-PA.

    Entry informationi

    Entry nameiPLEC_HUMAN
    AccessioniPrimary (citable) accession number: Q15149
    Secondary accession number(s): Q15148
    , Q16640, Q6S376, Q6S377, Q6S378, Q6S379, Q6S380, Q6S381, Q6S382, Q6S383
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 170 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3